glucosidase II is a glycan-processing enzyme that trims two alpha1,3-linked glucose residues from N-glycan on newly synthesized glycoproteins. Trimming of the first alpha1,3-linked glucose from Glc2Man9GlcNAc2 is important for a glycoprotein to interact with calnexin/calreticulin, and cleavage of the innermost glucose from GlcMan9GlcNAc2 sets glycoproteins free from the CNX/CRT cycle and allows them to proceed to the Golgi apparatus

glucosidase II plays a key role in glycoprotein biogenesis in the endoplasmic reticulum. It is responsible for the sequential removal of the two innermost glucose residues from the glycan, Glc3Man9GlcNAc2, transferred to Asn residues in proteins. The enzyme participates in the calnexin/calreticulin cycle, it removes the single glucose unit added to folding intermediates and misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase

glucosidase II plays a key role in glycoprotein biogenesis in the endoplasmic reticulum. It is responsible for the sequential removal of the two innermost glucose residues from the glycan, Glc3Man9GlcNAc2, transferred to Asn residues in proteins. The enzyme participates in the calnexin/calreticulin cycle, it removes the single glucose unit added to folding intermediates and misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase

alpha- and beta-subunits of endoplasmic reticulum resident glucosidase II are essential for stable accumulation and quality control of the elf18 receptor EFR but not the flg22 receptor FLS2, overview. Subunit GIIalpha mediates the catalytic activity of the enzyme whereas subunit GIIbeta directly interacts with and holds GIIalpha in the ER through its ER retention signal. Subunit GIIbeta is required for EFR-mediated anthocyanin repression

degradation of Streptococcus mutans biofilms only with structural integrity of the N-terminal Mutan-binding-domain and the C-terminal Mutanase-activity-domain separated by a characteristic sequence of proline and threonine repeats

degradation of Streptococcus mutans biofilms only with structural integrity of the N-terminal Mutan-binding-domain and the C-terminal Mutanase-activity-domain separated by a characteristic sequence of proline and threonine repeats

Catalyzes the hydrolysis of the inner two alpha-1,3-linked glucose residues present in all N-linked immature oligosaccharides, associates with and glycosylates the protein CD45, possible role in CD45 regulation

the mutanase also degrades alpha-1,3-polymers of biofilms, formed in vitro by Streptococcus mutans, even after only 3 min of contact. Maximum dissociation of adherent biofilm (64%) occurs at the highest enzyme concentration (2 units/ml)

the mutanase also degrades alpha-1,3-polymers of biofilms, formed in vitro by Streptococcus mutans, even after only 3 min of contact. Maximum dissociation of adherent biofilm (64%) occurs at the highest enzyme concentration (2 units/ml)

the GTB1 subunit of glucosidase II is required for glycoprotein processing in the endoplasmic reticulum, specifically required for the final glucose-trimming event during normal glycoprotein processing

degradation of Streptococcus mutans biofilms only with structural integrity of the N-terminal Mutan-binding-domain and the C-terminal Mutanase-activity-domain separated by a characteristic sequence of proline and threonine repeats

degradation of Streptococcus mutans biofilms only with structural integrity of the N-terminal Mutan-binding-domain and the C-terminal Mutanase-activity-domain separated by a characteristic sequence of proline and threonine repeats

Catalyzes the hydrolysis of the inner two alpha-1,3-linked glucose residues present in all N-linked immature oligosaccharides, associates with and glycosylates the protein CD45, possible role in CD45 regulation

the GTB1 subunit of glucosidase II is required for glycoprotein processing in the endoplasmic reticulum, specifically required for the final glucose-trimming event during normal glycoprotein processing

i.e. 6-bromo-3,4,5-trihydroxycyclohex-1-ene. In the presence of 0.3 mM bromoconduritol the cleavage-2 is strongly inhibited (the consumption of Glc1Man9GlcNAc2 is less than 10% even after 24 h). The consumption of Glc2Man9GlcNAc2 is about 20% after 1 h, while that in the absence of bromoconduritol is about 70%. For the cleavage-1, the extent of inhibition increases as the preincubation time elongates. The binding of bromoconduritol to glucosidase-II is an irreversible and slow process

the specific activity for degradation of Streptococcus mutans biofilms is 1.4 micromol/ml after incubation at 35°C at pH 6.0 for 3 min, degradation of Streptococcus mutans biofilms only with structural integrity of the N-terminal Mutan-binding-domain and the C-terminal Mutanase-activity-domain separated by a characteristic sequence of proline and threonine repeats

the specific activity for degradation of Streptococcus mutans biofilms is 1.4 micromol/ml after incubation at 35°C at pH 6.0 for 3 min, degradation of Streptococcus mutans biofilms only with structural integrity of the N-terminal Mutan-binding-domain and the C-terminal Mutanase-activity-domain separated by a characteristic sequence of proline and threonine repeats

the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for maltose as a substrate in cell extracts is 11fold higher during growth in YT medium (Brock’s mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing maltose, than during growth on other sugars

the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for maltose as a substrate in cell extracts is 11fold higher during growth in YT medium (Brock’s mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing maltose, than during growth on other sugars

the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for maltose as a substrate in cell extracts is 10fold higher during growth in YT medium (Brock’s mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing starch, than during growth on other sugars

the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for maltose as a substrate in cell extracts is 10fold higher during growth in YT medium (Brock’s mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing starch, than during growth on other sugars

alpha, beta, two different isoforms of the alpha subunit identified, alpha1 is the short and alpha2 the long isoform, both isoforms form dimers with the beta subunit, only dimeric form shows catalytic activity; alpha, beta, two different isoforms of the alpha subunit identified, alpha1 is the short and alpha2 the long isoforms, both isoforms forms dimers with the beta subunit, only dimeric form shows catalytic activity

the enzyme is a heterodimer whose alpha-subunit contains a glycosidase active site, while the beta-subunit confers the substrate specificity toward di- and monoglucosylated glycans on the glucose-trimming activity of the alpha-subunit

the enzyme is a heterodimer whose alpha-subunit GIIalpha bears the glycosyl hydrolase active site, whereas its beta-subunit GIIbeta is involved in GIIbeta endoplasmic reticulum retention and folding, but does not efficiently deglucosylate the physiological substrates Glc2Man9GlcNAc2 and Glc1Man9GlcNAc2

the enzyme is a heterodimer whose alpha-subunit GIIalpha bears the glycosyl hydrolase active site, whereas its beta-subunit GIIbeta is involved in GIIbeta endoplasmic reticulum retention and folding, but does not efficiently deglucosylate the physiological substrates Glc2Man9GlcNAc2 and GlcMan9GlcNAc2. GIIbeta is required for an efficient in vitro glucose trimming from G2M9 and G1M9, and processing of both middle and innermost glucoses

2-fold purification and 98% residual enzyme activity after precipitation with propanol, around 2-fold purification and 77% enzyme recovery after salting out with ammonium sulfate at 50% saturation, 10-fold concentrated preparation of the enzyme with a yield of 98% after ultrafiltration, mutanase recovery of 97% after lyophilization and concentration of the culture broth in a vacuum evaporator

construction of strains of gene disruptants lacking either the glucosidase II alpha- or beta-subunit. The mutant lacking the beta-subunit is inactive with both Glc2Man9GlcNAc2 and Glc1Man9GlcNAc2, but activity can be restored by adding the beta-subunit fraction, overview

a mutant enzyme with the mutant subunit IIbeta loses the sugar-binding activity of the GIIbeta-MRH domain, but hydrolyzes 4-nitrophenyl-alpha-glucopyranoside, although the capacity to remove glucose residues from G1M9 and G2M9 is significantly decreased, phenotype, overview

construction of alpha or beta-subunit deletion mutant strains, disruption of subunit GIIalpha leads to complete loss of enzyme activity, while in the absence of GIIbeta, the catalytic subunit GIIalpha of Schizosaccharomyces pombe folds to an active conformation able to hydrolyze 4-nitrophenyl alpha-D-glucopyranoside, phenotypes, overview

Biochemical and Molecular Characterization of a Novel Type of Mutanase from Paenibacillus sp. Strain RM: Identificatiion of its Mutan-Binding Domain, Essential for Degradation of Streptococcus mutans Biofilms